Evidence map›Paper›PMID 42402989›Full record

ArticleJournal of cell science2026

From the flagellum attachment zone to the tripartite attachment complex - widespread cytoskeletal engagement of T. brucei KMP11.

Salome Aeschlimann, Clirim Jetishi, Caroline E Dewar, Philip Stettler, Markus Gerber, Silke Oeljeklaus, Bettina Warscheid, Torsten Ochsenreiter, André Schneider

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of cell science, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors.

Salome AeschlimannDepartment of Chemistry, Biochemistry and Pharmaceutical Sciences, University of Bern, 3012 Bern, Switzerland.ORCID 0000-0002-7619-7001
Clirim JetishiInstitute of Cell Biology, University of Bern, 3012 Bern, Switzerland.
Caroline E DewarDivision of Biomedical and Life Sciences, Faculty of Health and Medicine (FHM), Lancaster University, Lancaster LA1 4YW, UK.
Philip StettlerDepartment of Chemistry, Biochemistry and Pharmaceutical Sciences, University of Bern, 3012 Bern, Switzerland.
Markus GerberInstitute of Cell Biology, University of Bern, 3012 Bern, Switzerland.ORCID 0009-0008-4994-7461
Silke OeljeklausFaculty of Chemistry and Pharmacy, Biochemistry II, Theodor Boveri-Institute, Biocenter, University of Würzburg, 97074 Würzburg, Germany.
Bettina WarscheidFaculty of Chemistry and Pharmacy, Biochemistry II, Theodor Boveri-Institute, Biocenter, University of Würzburg, 97074 Würzburg, Germany.
Torsten OchsenreiterInstitute of Cell Biology, University of Bern, 3012 Bern, Switzerland.ORCID 0000-0002-8846-8526
André SchneiderDepartment of Chemistry, Biochemistry and Pharmaceutical Sciences, University of Bern, 3012 Bern, Switzerland.ORCID 0000-0001-5421-0909

Funding

Canton of BernDeutsche Forschungsgemeinschaft 285767414Deutsche Forschungsgemeinschaft 541758684Deutsche Forschungsgemeinschaft GRK2243/2Deutsche Forschungsgemeinschaft SPP2453Schweizerischer Nationalfonds zur Forderung der Wissenschaftlichen Forschung 205601Schweizerischer Nationalfonds zur Forderung der Wissenschaftlichen Forschung 207525Swiss National Science Foundation 205601Swiss National Science Foundation SNF 205200Uniscientia FoundationWellcome Trust 205200
6 · The paper itself

Abstract

KMP11 is a conserved kinetoplastid protein yet its precise localization and function remained unclear. Using immunofluorescence, ultrastructure expansion microscopy (U-ExM), and proteomics, we comprehensively analyzed KMP11 in procyclic Trypanosoma brucei. Besides confirming localization to the flagellum attachment zone (FAZ), we identify previously unknown localizations at the paraflagellar rod (PFR), flagellar connector (FC), microtubule quartet (MtQ) and flagellar pocket collar/hook complex (FPC/HC) region. We further show that the previously described basal body localization corresponds to the tripartite attachment complex (TAC). Proteomic analyses identify multiple cytoskeletal interactors, including the TAC component p197. Immunoprecipitation and U-ExM analyses demonstrate that KMP11 associates with the central α-helical domain of p197 from both T. brucei and Trypanosoma cruzi. Furthermore, KMP11 interactors overall display significantly elevated α-helical content. Together, our findings establish KMP11 as a component of a broad cytoskeletal interaction network in trypanosomes and we speculate that KMP11 preferentially associates with α-helical proteins.

Indexed as

CytoskeletonFlagellaProtozoan ProteinsTrypanosoma brucei bruceiProtein BindingProtozoan ProteinsCytoskeletonmtDNA inheritanceT. bruceiTripartite attachment complexU-ExM

Identifiers

PMID42402989
PMCPMC13539426

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.